Related Experiment Video
Updated: Jul 4, 2026
07:37
Sorting of Streptomyces Cell Pellets Using a Complex Object Parametric Analyzer and Sorter
Published on: February 13, 2014
Pellet formation and cellular aggregation in Streptomyces tendae
S E Vecht-Lifshitz1, S Magdassi, S Braun
1Department of Biological Chemistry, Life Sciences Institute, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Biotechnology and Bioengineering
|April 15, 1990
Summary
Streptomyces tendae form pellets in submerged cultures. Pellet size is influenced by oxygen availability, which affects cell wall hydrophobicity and aggregation, with higher oxygen promoting pellet formation.
Area of Science:
- Microbiology
- Biotechnology
- Bioprocess Engineering
Background:
- Submerged cultures of Streptomyces tendae typically form noncoagulative, fluffy spherical pellets.
- Understanding factors influencing pellet formation is crucial for optimizing bioprocesses.
Purpose of the Study:
- To investigate the key factors affecting pellet size and morphology in Streptomyces tendae submerged cultures.
- To elucidate the role of cell wall hydrophobicity and dissolved oxygen in cellular aggregation.
Main Methods:
- Cultivation of Streptomyces tendae in submerged cultures under varying conditions.
- Manipulation of shear rate, pH, temperature, inoculum size, and dissolved oxygen levels.
- Assessment of pellet size, morphology, and cell wall hydrophobicity.
Main Results:
- Decreasing shear rate, pH, temperature, or inoculum size increased average pellet size.
- Oxygen limitation reduced pellet size and induced pulpy growth; oxygen sufficiency promoted pellet formation.
- Factors inducing pellet formation also increased cell wall hydrophobicity.
Conclusions:
- Hydrophobic interactions of cell walls are proposed as the primary forces driving cellular aggregation in Streptomyces tendae.
- Dissolved oxygen availability is a key regulator of these hydrophobic interactions and subsequent pellet formation.
More Related Videos
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:30Bacterial Phylum Actinobacteria
Coryneform bacteria are gram-positive, aerobic, nonmotile rods that exhibit irregular, club-shaped, or V-shaped arrangements. Their V-shape results from snapping division, where the inner cell wall layer forms the cross-wall, while the outer layer remains intact until it ruptures on one side, causing the daughter cells to bend away.The primary genera are Corynebacterium and Arthrobacter. Corynebacterium includes diverse species, ranging from saprophytes to pathogens like Corynebacterium...
01:22Protein Folding
Overview
01:13Actin Polymerization and Cell Motility
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.